Journal
SCIENTIFIC REPORTS
Volume 2, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/srep00843
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Funding
- Presidium of the Russian Academy of Sciences (Program Molecular and Cellular Biology to AAM)
- Estonian Science Foundation [7616, 9012, 6768, 9020]
- European Social Fund through Estonian Science Foundation [MJD99]
- Russian Foundation for Basic Research [10-04-01746-a]
- European Regional Development Fund through the Center of Excellence in Chemical Biology
- SA Archimedes PhD studies and DoRa6 programme grants
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Translational GTPases (trGTPases) are involved in all four stages of protein biosynthesis: initiation, elongation, termination and ribosome recycling. The trGTPases Initiation Factor 2 (IF2) and Elongation Factor G (EF-G) respectively orchestrate initiation complex formation and translocation of the peptidyl-tRNA: mRNA complex through the bacterial ribosome. The ribosome regulates the GTPase cycle and efficiently discriminates between the GDP- and GTP-bound forms of these proteins. Using Isothermal Titration Calorimetry, we have investigated interactions of IF2 and EF-G with the sarcin-ricin loop of the 23S rRNA, a crucial element of the GTPase-associated center of the ribosome. We show that binding of IF2 and EF-G to a 27 nucleotide RNA fragment mimicking the sarcin-ricin loop is mutually exclusive with that of GDP, but not of GTP, providing a mechanism for destabilization of the ribosome-bound GDP forms of translational GTPases.
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